Enzymes
| UniProtKB help_outline | 1,842 proteins |
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- Name help_outline a 2'-deoxyribonucleoside Identifier CHEBI:18274 Charge 0 Formula C5H9O3R SMILEShelp_outline OC[C@H]1O[C@@H]([*])C[C@@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 50 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline a ribonucleoside 5'-phosphate Identifier CHEBI:58043 Charge -2 Formula C5H8O7PR SMILEShelp_outline O[C@@H]1[C@H](O)[C@@H](COP([O-])([O-])=O)O[C@H]1[*] 2D coordinates Mol file for the small molecule Search links Involved in 760 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline a 2'-deoxyribonucleoside 5'-phosphate Identifier CHEBI:65317 Charge -2 Formula C5H8O6PR SMILEShelp_outline [C@H]1(O[C@H](COP([O-])(=O)[O-])[C@H](C1)O)* 2D coordinates Mol file for the small molecule Search links Involved in 80 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline a ribonucleoside Identifier CHEBI:18254 Charge 0 Formula C5H9O4R SMILEShelp_outline OC[C@H]1O[C@@H]([*])[C@H](O)[C@@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 205 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:19961 | RHEA:19962 | RHEA:19963 | RHEA:19964 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Related reactions help_outline
Specific form(s) of this reaction
Publications
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Nucleoside phosphotransferase from barley. Characterization and evidence for ping pong kinetics involving phosphoryl enzyme.
Prasher D.C., Carr M.C., Ives D.H., Tsai T.C., Frey P.A.
A nucleoside phosphotransferase has been purified to homogeneity from barley seedlings. Its Mr is about 50,000 and it consists of two subunits of equal size. A tightly bound metal ion required for activity can be replaced by Mg, Ba, or Co ions, but not by divalent Cu, Ca, Cd, or Hg. The enzyme is ... >> More
A nucleoside phosphotransferase has been purified to homogeneity from barley seedlings. Its Mr is about 50,000 and it consists of two subunits of equal size. A tightly bound metal ion required for activity can be replaced by Mg, Ba, or Co ions, but not by divalent Cu, Ca, Cd, or Hg. The enzyme is capable of catalyzing the transfer of phosphate from nucleoside monophosphates to the 5'-hydroxyl of any other nucleoside, but shows a decided preference for purine deoxynucleoside phosphate acceptors. A short lived phosphoryl enzyme intermediate has been trapped by rapid denaturation in presence of [32P]AMP. The steady state kinetics of this enzyme is found to be fully consistent with a branched ping pong pathway involving a compulsory phosphoryl enzyme intermediate from which phosphate may be transferred to nucleoside or to water. With appropriately chosen substrates, parallel line reciprocal plots were obtained, provided that both products of the branched pathway were taken into account in the rate measurements. Conversely, when only transphosphorylation was measured, converging reciprocal plots were obtained. Accordingly, assays were devised for the measurement of three velocity components: transphosphorylation, hydrolysis, and the sum of both reactions. Competitive inhibition of the transferase reaction by higher concentrations of either substrate is attributed to deadend interactions. Instead of being inhibited by the formation of a putative E-P.AMP complex, however, the phosphatase reaction is accelerated almost 2-fold. << Less
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Purification and properties of a nucleoside phosphotransferase from carrot.
Brunngraber E.F., Chargaff E.